ADX_RAT
ID ADX_RAT Reviewed; 188 AA.
AC P24483;
DT 01-MAR-1992, integrated into UniProtKB/Swiss-Prot.
DT 01-MAR-1992, sequence version 1.
DT 03-AUG-2022, entry version 146.
DE RecName: Full=Adrenodoxin, mitochondrial;
DE AltName: Full=Adrenal ferredoxin;
DE AltName: Full=Ferredoxin-1;
DE Flags: Precursor;
GN Name=Fdx1;
OS Rattus norvegicus (Rat).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Rattus.
OX NCBI_TaxID=10116;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RC TISSUE=Ovary;
RX PubMed=1863358; DOI=10.1089/dna.1991.10.339;
RA Mellon S.H., Kushner J.A., Vaisse C.;
RT "Expression and regulation of adrenodoxin and P450scc mRNA in rodent
RT tissues.";
RL DNA Cell Biol. 10:339-347(1991).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA].
RC STRAIN=Wistar; TISSUE=Adrenal gland;
RX PubMed=8820908; DOI=10.1248/bpb.19.39;
RA Sagara Y., Watanabe Y., Kawamura K., Yubisui T.;
RT "Cloning and sequence analysis of a full-length cDNA of rat adrenodoxin.";
RL Biol. Pharm. Bull. 19:39-41(1996).
RN [3]
RP SUBCELLULAR LOCATION.
RX PubMed=2170421; DOI=10.1083/jcb.111.4.1373;
RA Hanukoglu I., Suh B.S., Himmelhoch S., Amsterdam A.;
RT "Induction and mitochondrial localization of cytochrome P450scc system
RT enzymes in normal and transformed ovarian granulosa cells.";
RL J. Cell Biol. 111:1373-1381(1990).
CC -!- FUNCTION: Essential for the synthesis of various steroid hormones.
CC Participates in the reduction of mitochondrial cytochrome P450 for
CC steroidogenesis. Transfers electrons from adrenodoxin reductase to
CC CYP11A1, a cytochrome P450 that catalyzes cholesterol side-chain
CC cleavage. Does not form a ternary complex with adrenodoxin reductase
CC and CYP11A1 but shuttles between the two enzymes to transfer electrons.
CC {ECO:0000250|UniProtKB:P00257}.
CC -!- COFACTOR:
CC Name=[2Fe-2S] cluster; Xref=ChEBI:CHEBI:190135;
CC Note=Binds 1 [2Fe-2S] cluster.;
CC -!- SUBUNIT: Interacts with CYP11A1. {ECO:0000250|UniProtKB:P10109}.
CC -!- SUBCELLULAR LOCATION: Mitochondrion matrix
CC {ECO:0000269|PubMed:2170421}.
CC -!- TISSUE SPECIFICITY: Found in all tissues, most abundant in adrenals,
CC ovaries and testes.
CC -!- SIMILARITY: Belongs to the adrenodoxin/putidaredoxin family.
CC {ECO:0000305}.
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DR EMBL; D50436; BAA08927.1; -; mRNA.
DR PIR; A39553; A39553.
DR RefSeq; NP_058822.1; NM_017126.1.
DR AlphaFoldDB; P24483; -.
DR SMR; P24483; -.
DR STRING; 10116.ENSRNOP00000016263; -.
DR iPTMnet; P24483; -.
DR PhosphoSitePlus; P24483; -.
DR PaxDb; P24483; -.
DR PRIDE; P24483; -.
DR GeneID; 29189; -.
DR KEGG; rno:29189; -.
DR UCSC; RGD:62036; rat.
DR CTD; 2230; -.
DR RGD; 62036; Fdx1.
DR eggNOG; KOG3309; Eukaryota.
DR InParanoid; P24483; -.
DR OrthoDB; 1380051at2759; -.
DR PhylomeDB; P24483; -.
DR Reactome; R-RNO-1362409; Mitochondrial iron-sulfur cluster biogenesis.
DR Reactome; R-RNO-196108; Pregnenolone biosynthesis.
DR Reactome; R-RNO-211976; Endogenous sterols.
DR Reactome; R-RNO-2395516; Electron transport from NADPH to Ferredoxin.
DR PRO; PR:P24483; -.
DR Proteomes; UP000002494; Unplaced.
DR GO; GO:0030061; C:mitochondrial crista; IDA:RGD.
DR GO; GO:0005759; C:mitochondrial matrix; IDA:UniProtKB.
DR GO; GO:0005739; C:mitochondrion; IDA:RGD.
DR GO; GO:0051537; F:2 iron, 2 sulfur cluster binding; ISS:UniProtKB.
DR GO; GO:0009055; F:electron transfer activity; IDA:RGD.
DR GO; GO:0019899; F:enzyme binding; IPI:RGD.
DR GO; GO:0005506; F:iron ion binding; IDA:RGD.
DR GO; GO:0030325; P:adrenal gland development; IEP:RGD.
DR GO; GO:0071320; P:cellular response to cAMP; ISO:RGD.
DR GO; GO:0071872; P:cellular response to epinephrine stimulus; IEP:RGD.
DR GO; GO:1904322; P:cellular response to forskolin; ISO:RGD.
DR GO; GO:0044320; P:cellular response to leptin stimulus; IEP:RGD.
DR GO; GO:0071407; P:cellular response to organic cyclic compound; IEP:RGD.
DR GO; GO:0008203; P:cholesterol metabolic process; ISS:UniProtKB.
DR GO; GO:0022900; P:electron transport chain; IBA:GO_Central.
DR GO; GO:0042446; P:hormone biosynthetic process; ISS:UniProtKB.
DR GO; GO:0070995; P:NADPH oxidation; IDA:RGD.
DR GO; GO:0140647; P:P450-containing electron transport chain; IEA:InterPro.
DR GO; GO:0051353; P:positive regulation of oxidoreductase activity; IMP:RGD.
DR GO; GO:0050790; P:regulation of catalytic activity; IDA:RGD.
DR GO; GO:0034698; P:response to gonadotropin; IEP:RGD.
DR GO; GO:0044321; P:response to leptin; IEP:RGD.
DR GO; GO:0006694; P:steroid biosynthetic process; IEA:UniProtKB-KW.
DR CDD; cd00207; fer2; 1.
DR Gene3D; 3.10.20.30; -; 1.
DR InterPro; IPR036010; 2Fe-2S_ferredoxin-like_sf.
DR InterPro; IPR001041; 2Fe-2S_ferredoxin-type.
DR InterPro; IPR001055; Adrenodoxin.
DR InterPro; IPR018298; Adrenodoxin_Fe-S_BS.
DR InterPro; IPR012675; Beta-grasp_dom_sf.
DR PANTHER; PTHR23426; PTHR23426; 1.
DR Pfam; PF00111; Fer2; 1.
DR PRINTS; PR00355; ADRENODOXIN.
DR SUPFAM; SSF54292; SSF54292; 1.
DR PROSITE; PS51085; 2FE2S_FER_2; 1.
DR PROSITE; PS00814; ADX; 1.
PE 2: Evidence at transcript level;
KW 2Fe-2S; Acetylation; Cholesterol metabolism; Electron transport; Iron;
KW Iron-sulfur; Lipid metabolism; Metal-binding; Mitochondrion;
KW Phosphoprotein; Reference proteome; Steroid metabolism; Steroidogenesis;
KW Sterol metabolism; Transit peptide; Transport.
FT TRANSIT 1..64
FT /note="Mitochondrion"
FT CHAIN 65..188
FT /note="Adrenodoxin, mitochondrial"
FT /id="PRO_0000000991"
FT DOMAIN 69..175
FT /note="2Fe-2S ferredoxin-type"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00465"
FT BINDING 110
FT /ligand="[2Fe-2S] cluster"
FT /ligand_id="ChEBI:CHEBI:190135"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00465"
FT BINDING 116
FT /ligand="[2Fe-2S] cluster"
FT /ligand_id="ChEBI:CHEBI:190135"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00465"
FT BINDING 119
FT /ligand="[2Fe-2S] cluster"
FT /ligand_id="ChEBI:CHEBI:190135"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00465"
FT BINDING 156
FT /ligand="[2Fe-2S] cluster"
FT /ligand_id="ChEBI:CHEBI:190135"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00465"
FT MOD_RES 67
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P46656"
FT MOD_RES 70
FT /note="N6-acetyllysine; alternate"
FT /evidence="ECO:0000250|UniProtKB:P46656"
FT MOD_RES 70
FT /note="N6-succinyllysine; alternate"
FT /evidence="ECO:0000250|UniProtKB:P46656"
FT MOD_RES 162
FT /note="N6-succinyllysine"
FT /evidence="ECO:0000250|UniProtKB:P46656"
FT MOD_RES 181
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P10109"
SQ SEQUENCE 188 AA; 20135 MW; B0686D5159A30240 CRC64;
MAAAPGARLL RAACASVAFR GLDCRRLLVC GTRAGPAVPQ WTPSPHTLAE AGPGRPLSVS
ARARSSSEDK VTVHFKNRDG ETLTTKGKVG DSLLDVVIEN NLDIDGFGAC EGTLACSTCH
LIFEDHIYEK LDAITDEEND MLDLAFGLTN RSRLGCQVCL TKAMDNMTVR VPEAVADVRQ
SVDMSKNS
